2. Academic Validation
  3. Protein Prenyltransferases and Their Inhibitors: Structural and Functional Characterization

Protein Prenyltransferases and Their Inhibitors: Structural and Functional Characterization

  • Int J Mol Sci. 2022 May 12;23(10):5424. doi: 10.3390/ijms23105424.
Aleksandra Marchwicka 1,  Daria Kamińska 1,  Mohsen Monirialamdari 2,  Katarzyna M Błażewska 2,  Edyta Gendaszewska-Darmach 1
Affiliations

Affiliations

  • 1 Institute of Molecular and Industrial Biotechnology, Faculty of Biotechnology and Food Sciences, Lodz University of Technology, 90-537 Lodz, Poland.
  • 2 Institute of Organic Chemistry, Faculty of Chemistry, Lodz University of Technology, 90-924 Lodz, Poland.
PMID: 35628237 DOI: 10.3390/ijms23105424
Abstract

Protein prenylation is a post-translational modification controlling the localization, activity, and protein-protein interactions of small GTPases, including the Ras superfamily. This covalent attachment of either a farnesyl (15 carbon) or a geranylgeranyl (20 carbon) isoprenoid group is catalyzed by four prenyltransferases, namely farnesyltransferase (FTase), geranylgeranyltransferase type I (GGTase-I), Rab geranylgeranyltransferase (GGTase-II), and recently discovered geranylgeranyltransferase type III (GGTase-III). Blocking small GTPase activity, namely inhibiting prenyltransferases, has been proposed as a potential disease treatment method. Inhibitors of prenyltransferase have resulted in substantial therapeutic benefits in various diseases, such as Cancer, neurological disorders, and viral and parasitic infections. In this review, we overview the structure of FTase, GGTase-I, GGTase-II, and GGTase-III and summarize the current status of research on their inhibitors.

Keywords

inhibitors; prenyltransferases; structures.

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